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Literature summary extracted from

  • Guo, Q.; Zhao, F.; Guo, S.Y.; Wang, X.
    The tryptophane residues of dimeric arginine kinase: roles of Trp-208 and Trp-218 in active site and conformation stability (2004), Biochimie, 86, 379-386.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
2.7.3.3 W208A mutant enzyme shows 70.3% of the wild-type enzyme in the forward reaction. Mutation makes the enzyme susceptible to heat and denaturants, sich as guanidine HCl Apostichopus japonicus
2.7.3.3 W218A mutation causes almost complete loss of activity and decreases the melting temperature in differential scanning calometry profiles and decreases stability against guanidine hydrochloride denaturation Apostichopus japonicus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.3.3 0.33
-
 ATP pH 8.1, mutant enzyme W208A Apostichopus japonicus
2.7.3.3 0.48
-
 ATP pH 8.1, wild-type enzyme Apostichopus japonicus
2.7.3.3 0.66
-
 L-arginine pH 8.1, wild-type enzyme Apostichopus japonicus
2.7.3.3 0.7
-
 L-arginine pH 8.1, mutant enzyme W208A Apostichopus japonicus

Organism

EC Number Organism UniProt Comment Textmining
2.7.3.3 Apostichopus japonicus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.3.3
-
 Apostichopus japonicus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.3.3 ATP + L-arginine
-
 Apostichopus japonicus ADP + Nomega-phosphono-L-arginine
-
 ?